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4dt1

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Current revision (08:48, 20 March 2024) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dt1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DT1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dt1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DT1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DT1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.899&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dt1 OCA], [https://pdbe.org/4dt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dt1 RCSB], [https://www.ebi.ac.uk/pdbsum/4dt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dt1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4dt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dt1 OCA], [https://pdbe.org/4dt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dt1 RCSB], [https://www.ebi.ac.uk/pdbsum/4dt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dt1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CSM2_YEAST CSM2_YEAST]] Involved in chromosome segregation during meiosis. Promotes efficient recombinational repair and functions in the protection of the genome from spontaneous and induced DNA damage like mutations and gross chromosomal rearrangements (GCRs).<ref>PMID:11470404</ref> <ref>PMID:12972632</ref> <ref>PMID:15184655</ref> <ref>PMID:15654096</ref> <ref>PMID:19496932</ref>
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[https://www.uniprot.org/uniprot/CSM2_YEAST CSM2_YEAST] Involved in chromosome segregation during meiosis. Promotes efficient recombinational repair and functions in the protection of the genome from spontaneous and induced DNA damage like mutations and gross chromosomal rearrangements (GCRs).<ref>PMID:11470404</ref> <ref>PMID:12972632</ref> <ref>PMID:15184655</ref> <ref>PMID:15654096</ref> <ref>PMID:19496932</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The yeast Shu complex, consisting of the proteins Shu1, Shu2, Psy3, and Csm2, maintains genomic stability by coupling post-replication repair to homologous recombination. However, a lack of biochemical and structural information on the Shu proteins precludes revealing their precise roles within the pathway. Here, we report on the 1.9-A crystal structure of the Psy3-Csm2 complex. The crystal structure shows that Psy3 forms a heterodimer with Csm2 mainly through a hydrophobic core. Unexpectedly, Psy3 and Csm2 share a similar architecture that closely resembles the ATPase core domain of Rad51. The L2 loop present in Psy3 and Csm2 is similar to that of Rad51 and confers the DNA binding activity of the Shu complex. As with Rad51, the Shu complex appears to form a nucleoprotein filament by binding nonspecifically to DNA. Structure-based mutagenesis studies have demonstrated that the DNA binding activity of the Shu complex is essential for repair of the methyl methanesulfonate-induced DNA damage. Our findings provide good foundations for the understanding of the Srs2 regulation by the Shu complex.
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Structural analysis of Shu proteins reveals a DNA binding role essential for resisting damage.,Tao Y, Li X, Liu Y, Ruan J, Qi S, Niu L, Teng M J Biol Chem. 2012 Jun 8;287(24):20231-9. doi: 10.1074/jbc.M111.334698. Epub 2012 , Mar 30. PMID:22465956<ref>PMID:22465956</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dt1" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>

Current revision

Crystal structure of the Psy3-Csm2 complex

PDB ID 4dt1

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